Inside Back Cover: "Head‐to‐Middle" and "Head‐to‐Tail" cis‐Prenyl Transferases: Structure of Isosesquilavandulyl Diphosphate Synthase (Angew. Chem. Int. Ed. 3/2018). Issue 3 (28th December 2017)

• Record Type: Journal Article
• Authors: Gao, Jian; Ko, Tzu‐Ping; Chen, Lu; Malwal, Satish R.; Zhang, Jianan; Hu, Xiangying; Qu, Fiona; Liu, Weidong; Huang, Jian‐Wen; Cheng, Ya‐Shan; Chen, Chun‐Chi; Yang, Yunyun; Zhang, Yonghui; Oldfield, Eric; Guo, Rey‐Ting
• Is Part Of: Angewandte Chemie international edition. Volume 57:Issue 3(2018)
• Page Start: 851
• Page End: 851
• Publication Date: 2017-12-28
• Subjects: antibiotics -- enzymes -- isoprenoids -- protein structures -- X-ray diffraction; Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.201712846
• Languages: English
• ISSNs: 1433-7851

Abstract

Abstract : The condensation of dimethylallyl diphosphate and geranyl diphosphate is catalyzed by isosesquilavandulyl diphosphate synthase (mcl22) from Streptomyces CNH‐189 through a recently classified head‐to‐middle mechanism, producing a precursor of novel merochlorin‐class antibiotics. In their Communication onpage 683 ff., R.‐T. Guo et al. present crystal structures of mcl22 in complex with substrate analogues. Mcl22 forms an unprecedented pocket to accommodate the allylic substrate.